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Volumn 6, Issue 4, 2011, Pages

Single molecule In Vivo analysis of toll-like receptor 9 and CpG DNA interaction

Author keywords

[No Author keywords available]

Indexed keywords

DNA; GREEN FLUORESCENT PROTEIN; OLIGONUCLEOTIDE; TOLL LIKE RECEPTOR 9; LIGAND;

EID: 79953679912     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0017991     Document Type: Article
Times cited : (34)

References (39)
  • 1
    • 0036954037 scopus 로고    scopus 로고
    • Recognition of lipopeptides by Toll-like receptors
    • Takeda K, Takeuchi O, Akira S, (2002) Recognition of lipopeptides by Toll-like receptors. J Endotoxin Res 8: 459-463.
    • (2002) J Endotoxin Res , vol.8 , pp. 459-463
    • Takeda, K.1    Takeuchi, O.2    Akira, S.3
  • 2
    • 35549006674 scopus 로고    scopus 로고
    • The Drosophila systemic immune response: sensing and signalling during bacterial and fungal infections
    • Ferrandon D, Imler JL, Hetru C, Hoffmann JA, (2007) The Drosophila systemic immune response: sensing and signalling during bacterial and fungal infections. Nat Rev Immunol 7: 862-874.
    • (2007) Nat Rev Immunol , vol.7 , pp. 862-874
    • Ferrandon, D.1    Imler, J.L.2    Hetru, C.3    Hoffmann, J.A.4
  • 3
    • 0036318851 scopus 로고    scopus 로고
    • Bacterial CpG-DNA and lipopolysaccharides activate Toll-like receptors at distinct cellular compartments
    • Ahmad-Nejad P, Hacker H, Rutz M, Bauer S, Vabulas RM, et al. (2002) Bacterial CpG-DNA and lipopolysaccharides activate Toll-like receptors at distinct cellular compartments. Eur J Immunol 32: 1958-1968.
    • (2002) Eur J Immunol , vol.32 , pp. 1958-1968
    • Ahmad-Nejad, P.1    Hacker, H.2    Rutz, M.3    Bauer, S.4    Vabulas, R.M.5
  • 4
    • 33746545577 scopus 로고    scopus 로고
    • Toll-like receptor 3 associates with c-Src tyrosine kinase on endosomes to initiate antiviral signaling
    • Johnsen IB, Nguyen TT, Ringdal M, Tryggestad AM, Bakke O, et al. (2006) Toll-like receptor 3 associates with c-Src tyrosine kinase on endosomes to initiate antiviral signaling. EMBO J 25: 3335-3346.
    • (2006) EMBO J , vol.25 , pp. 3335-3346
    • Johnsen, I.B.1    Nguyen, T.T.2    Ringdal, M.3    Tryggestad, A.M.4    Bakke, O.5
  • 5
    • 1542317578 scopus 로고    scopus 로고
    • Species-specific recognition of single-stranded RNA via toll-like receptor 7 and 8
    • Heil F, Hemmi H, Hochrein H, Ampenberger F, Kirschning C, et al. (2004) Species-specific recognition of single-stranded RNA via toll-like receptor 7 and 8. Science 303: 1526-1529.
    • (2004) Science , vol.303 , pp. 1526-1529
    • Heil, F.1    Hemmi, H.2    Hochrein, H.3    Ampenberger, F.4    Kirschning, C.5
  • 6
    • 0033968116 scopus 로고    scopus 로고
    • Endotoxin, toll-like receptor 4, and the afferent limb of innate immunity
    • Beutler B, (2000) Endotoxin, toll-like receptor 4, and the afferent limb of innate immunity. Curr Opin Microbiol 3: 23-28.
    • (2000) Curr Opin Microbiol , vol.3 , pp. 23-28
    • Beutler, B.1
  • 7
    • 0028931102 scopus 로고
    • CpG motifs in bacterial DNA trigger direct B-cell activation
    • Krieg AM, Yi AK, Matson S, Waldschmidt TJ, Bishop GA, et al. (1995) CpG motifs in bacterial DNA trigger direct B-cell activation. Nature 374: 546-549.
    • (1995) Nature , vol.374 , pp. 546-549
    • Krieg, A.M.1    Yi, A.K.2    Matson, S.3    Waldschmidt, T.J.4    Bishop, G.A.5
  • 8
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signalling
    • Akira S, Takeda K, (2004) Toll-like receptor signalling. Nat Rev Immunol 4: 499-511.
    • (2004) Nat Rev Immunol , vol.4 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 10
    • 4644330955 scopus 로고    scopus 로고
    • Toll-like receptor 9 binds single-stranded CpG-DNA in a sequence- and pH-dependent manner
    • Rutz M, Metzger J, Gellert T, Luppa P, Lipford GB, et al. (2004) Toll-like receptor 9 binds single-stranded CpG-DNA in a sequence- and pH-dependent manner. Eur J Immunol 34: 2541-2550.
    • (2004) Eur J Immunol , vol.34 , pp. 2541-2550
    • Rutz, M.1    Metzger, J.2    Gellert, T.3    Luppa, P.4    Lipford, G.B.5
  • 11
    • 32944462310 scopus 로고    scopus 로고
    • CpG motif-independent activation of TLR9 upon endosomal translocation of "natural" phosphodiester DNA
    • Yasuda K, Rutz M, Schlatter B, Metzger J, Luppa PB, et al. (2006) CpG motif-independent activation of TLR9 upon endosomal translocation of "natural" phosphodiester DNA. Eur J Immunol 36: 431-436.
    • (2006) Eur J Immunol , vol.36 , pp. 431-436
    • Yasuda, K.1    Rutz, M.2    Schlatter, B.3    Metzger, J.4    Luppa, P.B.5
  • 12
    • 34347218249 scopus 로고    scopus 로고
    • Nucleic acids exert a sequence-independent cooperative effect on sequence-dependent activation of Toll-like receptor 9
    • Kindrachuk J, Potter JE, Brownlie R, Ficzycz AD, Griebel PJ, et al. (2007) Nucleic acids exert a sequence-independent cooperative effect on sequence-dependent activation of Toll-like receptor 9. J Biol Chem 282: 13944-13953.
    • (2007) J Biol Chem , vol.282 , pp. 13944-13953
    • Kindrachuk, J.1    Potter, J.E.2    Brownlie, R.3    Ficzycz, A.D.4    Griebel, P.J.5
  • 13
    • 40249088259 scopus 로고    scopus 로고
    • The DNA sugar backbone 2′ deoxyribose determines toll-like receptor 9 activation
    • Haas T, Metzger J, Schmitz F, Heit A, Muller T, et al. (2008) The DNA sugar backbone 2′ deoxyribose determines toll-like receptor 9 activation. Immunity 28: 315-323.
    • (2008) Immunity , vol.28 , pp. 315-323
    • Haas, T.1    Metzger, J.2    Schmitz, F.3    Heit, A.4    Muller, T.5
  • 14
    • 34250698370 scopus 로고    scopus 로고
    • Ligand-induced conformational changes allosterically activate Toll-like receptor 9
    • Latz E, Verma A, Visintin A, Gong M, Sirois CM, et al. (2007) Ligand-induced conformational changes allosterically activate Toll-like receptor 9. Nat Immunol 8: 772-779.
    • (2007) Nat Immunol , vol.8 , pp. 772-779
    • Latz, E.1    Verma, A.2    Visintin, A.3    Gong, M.4    Sirois, C.M.5
  • 15
    • 0004120067 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy: theory and applications
    • New York, Springer, xx
    • Rigler R, Elson E, (2001) Fluorescence correlation spectroscopy: theory and applications. New York Springer xx pp. 487 p.
    • (2001) , pp. 487
    • Rigler, R.1    Elson, E.2
  • 16
    • 0030671161 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy: diagnostics for sparse molecules
    • Maiti S, Haupts U, Webb WW, (1997) Fluorescence correlation spectroscopy: diagnostics for sparse molecules. Proc Natl Acad Sci U S A 94: 11753-11757.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 11753-11757
    • Maiti, S.1    Haupts, U.2    Webb, W.W.3
  • 17
    • 73849138217 scopus 로고    scopus 로고
    • Quantitative investigation of compartmentalized dynamics of ErbB2 targeting gold nanorods in live cells by single molecule spectroscopy
    • Chen J, Irudayaraj J, (2009) Quantitative investigation of compartmentalized dynamics of ErbB2 targeting gold nanorods in live cells by single molecule spectroscopy. ACS Nano 3: 4071-4079.
    • (2009) ACS Nano , vol.3 , pp. 4071-4079
    • Chen, J.1    Irudayaraj, J.2
  • 18
    • 0030895059 scopus 로고    scopus 로고
    • Dual-color fluorescence cross-correlation spectroscopy for multicomponent diffusional analysis in solution
    • Schwille P, Meyer-Almes FJ, Rigler R, (1997) Dual-color fluorescence cross-correlation spectroscopy for multicomponent diffusional analysis in solution. Biophys J 72: 1878-1886.
    • (1997) Biophys J , vol.72 , pp. 1878-1886
    • Schwille, P.1    Meyer-Almes, F.J.2    Rigler, R.3
  • 19
    • 35748931313 scopus 로고    scopus 로고
    • Practical guidelines for dual-color fluorescence cross-correlation spectroscopy
    • Bacia K, Schwille P, (2007) Practical guidelines for dual-color fluorescence cross-correlation spectroscopy. Nat Protoc 2: 2842-2856.
    • (2007) Nat Protoc , vol.2 , pp. 2842-2856
    • Bacia, K.1    Schwille, P.2
  • 20
    • 77955153041 scopus 로고    scopus 로고
    • Fluorescence Lifetime Cross Correlation Spectroscopy Resolves EGFR and Antagonist Interaction in Live Cells
    • Chen J, Irudayaraj J, (2010) Fluorescence Lifetime Cross Correlation Spectroscopy Resolves EGFR and Antagonist Interaction in Live Cells. Analytical Chemistry 82: 6415-6421.
    • (2010) Analytical Chemistry , vol.82 , pp. 6415-6421
    • Chen, J.1    Irudayaraj, J.2
  • 21
    • 0344603641 scopus 로고    scopus 로고
    • The photon counting histogram in fluorescence fluctuation spectroscopy
    • Chen Y, Muller JD, So PT, Gratton E, (1999) The photon counting histogram in fluorescence fluctuation spectroscopy. Biophys J 77: 553-567.
    • (1999) Biophys J , vol.77 , pp. 553-567
    • Chen, Y.1    Muller, J.D.2    So, P.T.3    Gratton, E.4
  • 24
    • 3242776258 scopus 로고    scopus 로고
    • MD-2: the Toll 'gatekeeper' in endotoxin signalling
    • Gangloff M, Gay NJ, (2004) MD-2: the Toll 'gatekeeper' in endotoxin signalling. Trends Biochem Sci 29: 294-300.
    • (2004) Trends Biochem Sci , vol.29 , pp. 294-300
    • Gangloff, M.1    Gay, N.J.2
  • 26
    • 43149091227 scopus 로고    scopus 로고
    • Refractive index sensing of green fluorescent proteins in living cells using fluorescence lifetime imaging microscopy
    • van Manen HJ, Verkuijlen P, Wittendorp P, Subramaniam V, van den Berg TK, et al. (2008) Refractive index sensing of green fluorescent proteins in living cells using fluorescence lifetime imaging microscopy. Biophys J 94: L67-69.
    • (2008) Biophys J , vol.94
    • van Manen, H.J.1    Verkuijlen, P.2    Wittendorp, P.3    Subramaniam, V.4    van den Berg, T.K.5
  • 28
    • 27744475701 scopus 로고    scopus 로고
    • Anomalous diffusion of proteins due to molecular crowding
    • Banks DS, Fradin C, (2005) Anomalous diffusion of proteins due to molecular crowding. Biophys J 89: 2960-2971.
    • (2005) Biophys J , vol.89 , pp. 2960-2971
    • Banks, D.S.1    Fradin, C.2
  • 30
    • 0037342671 scopus 로고    scopus 로고
    • Measuring size distribution in highly heterogeneous systems with fluorescence correlation spectroscopy
    • Sengupta P, Garai K, Balaji J, Periasamy N, Maiti S, (2003) Measuring size distribution in highly heterogeneous systems with fluorescence correlation spectroscopy. Biophys J 84: 1977-1984.
    • (2003) Biophys J , vol.84 , pp. 1977-1984
    • Sengupta, P.1    Garai, K.2    Balaji, J.3    Periasamy, N.4    Maiti, S.5
  • 31
    • 0742289969 scopus 로고    scopus 로고
    • Signal transduction pathways mediated by the interaction of CpG DNA with Toll-like receptor 9
    • Takeshita F, Gursel I, Ishii KJ, Suzuki K, Gursel M, et al. (2004) Signal transduction pathways mediated by the interaction of CpG DNA with Toll-like receptor 9. Semin Immunol 16: 17-22.
    • (2004) Semin Immunol , vol.16 , pp. 17-22
    • Takeshita, F.1    Gursel, I.2    Ishii, K.J.3    Suzuki, K.4    Gursel, M.5
  • 32
    • 48749085127 scopus 로고    scopus 로고
    • Plasmacytoid dendritic cells: sensing nucleic acids in viral infection and autoimmune diseases
    • Gilliet M, Cao W, Liu YJ, (2008) Plasmacytoid dendritic cells: sensing nucleic acids in viral infection and autoimmune diseases. Nat Rev Immunol 8: 594-606.
    • (2008) Nat Rev Immunol , vol.8 , pp. 594-606
    • Gilliet, M.1    Cao, W.2    Liu, Y.J.3
  • 33
    • 0346734134 scopus 로고    scopus 로고
    • Probing protein oligomerization in living cells with fluorescence fluctuation spectroscopy
    • Chen Y, Wei LN, Muller JD, (2003) Probing protein oligomerization in living cells with fluorescence fluctuation spectroscopy. Proc Natl Acad Sci U S A 100: 15492-15497.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 15492-15497
    • Chen, Y.1    Wei, L.N.2    Muller, J.D.3
  • 34
    • 44349192634 scopus 로고    scopus 로고
    • SAM domain-based protein oligomerization observed by live-cell fluorescence fluctuation spectroscopy
    • Slaughter BD, Huff JM, Wiegraebe W, Schwartz JW, Li R, (2008) SAM domain-based protein oligomerization observed by live-cell fluorescence fluctuation spectroscopy. PLoS One 3: e1931.
    • (2008) PLoS One , vol.3
    • Slaughter, B.D.1    Huff, J.M.2    Wiegraebe, W.3    Schwartz, J.W.4    Li, R.5
  • 36
    • 0032476602 scopus 로고    scopus 로고
    • CpG-DNA-specific activation of antigen-presenting cells requires stress kinase activity and is preceded by non-specific endocytosis and endosomal maturation
    • Hacker H, Mischak H, Miethke T, Liptay S, Schmid R, et al. (1998) CpG-DNA-specific activation of antigen-presenting cells requires stress kinase activity and is preceded by non-specific endocytosis and endosomal maturation. EMBO J 17: 6230-6240.
    • (1998) EMBO J , vol.17 , pp. 6230-6240
    • Hacker, H.1    Mischak, H.2    Miethke, T.3    Liptay, S.4    Schmid, R.5
  • 37
    • 67649232601 scopus 로고    scopus 로고
    • Identification of an N-terminal recognition site in TLR9 that contributes to CpG-DNA-mediated receptor activation
    • Peter ME, Kubarenko AV, Weber AN, Dalpke AH, (2009) Identification of an N-terminal recognition site in TLR9 that contributes to CpG-DNA-mediated receptor activation. J Immunol 182: 7690-7697.
    • (2009) J Immunol , vol.182 , pp. 7690-7697
    • Peter, M.E.1    Kubarenko, A.V.2    Weber, A.N.3    Dalpke, A.H.4
  • 38
    • 3142697714 scopus 로고    scopus 로고
    • TLR9 is localized in the endoplasmic reticulum prior to stimulation
    • Leifer CA, Kennedy MN, Mazzoni A, Lee C, Kruhlak MJ, et al. (2004) TLR9 is localized in the endoplasmic reticulum prior to stimulation. J Immunol 173: 1179-1183.
    • (2004) J Immunol , vol.173 , pp. 1179-1183
    • Leifer, C.A.1    Kennedy, M.N.2    Mazzoni, A.3    Lee, C.4    Kruhlak, M.J.5
  • 39
    • 38049181017 scopus 로고    scopus 로고
    • Mapping dynamic protein interactions in MAP kinase signaling using live-cell fluorescence fluctuation spectroscopy and imaging
    • Slaughter BD, Schwartz JW, Li R, (2007) Mapping dynamic protein interactions in MAP kinase signaling using live-cell fluorescence fluctuation spectroscopy and imaging. Proc Natl Acad Sci U S A 104: 20320-20325.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 20320-20325
    • Slaughter, B.D.1    Schwartz, J.W.2    Li, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.